BSCI-1510 Lecture Notes - Lecture 5: Beta Barrel, Ribbon Diagram, Alpha Helix

26 views3 pages

skytoad282

10 Feb 2016

School

Vanderbilt University

Department

Biological Sciences

Course

BSCI-1510

Professor

Patton Jim

For unlimited access to Class Notes, a Class+ subscription is required.

Document Summary

Elements of protein structure: primary sequence of amino acids, secondary alpha helix & beta sheet, tertiary 3d conformation of a polypeptide, quaternary subunit composition. Most compact structure that a polypeptide can form. Hydrogen bonds hold alpha helix between carbonyl carbon and. Certain amino acids + sequence of amino acids can prevent alpha helix from forming. Arrows of beta sheet show direction of polarity. Most spread out a polypeptide can form. Antiparallel beta sheets have adjacent backbones that run in. R groups alternate what side of the antiparallel sheet they are opposite directions going to be on. Hydrogen groups are on the inside and r groups on the outside to avoid disruption of hydrogen bonds. Made of beta sheets that form beta barrel structure. Hydrophobic outside and hydrophilic inside = water filled barrel. Beta turns reverse orientation of polypeptide chain. Shows how polypeptide backbone winds in 3d space.

Related Questions

1. A sequence of amino acids in a certain protein is found to be â Ser â Gly â Pro â Gly â

The sequence is most probably part of a(n):

a. beta turn

b. antiparallel beta sheet

c. alpha-helix

d. parallel beta-sheet

e. alapha-sheet

2. Which statement about peptides bonds is NOT TRUE?

There is perfectly free rotation about the peptide bond.

The peptide bond has partial double-bond character.

The peptide bond is shorter than a normal carbon-nitrogen single bond.

The peptide bond usually has a trans configuration with respect to the alpha-carbons of the two amino acids involved in the peptide bond.

Peptide bonds are made via condensation of an amine and a carboxylic acid with loss of water.

3. Which of the following statements about proteins is FALSE?

	Active proteins are generally very loosely structured.
	In water-soluble proteins, hydrophobic amino acid residues are generally buried and not exposed to water.
	Primary structure determines tertiary structure.
	Secondary structure is regular, recurring arrangements in space of nearby amino acid residues in a polypeptide.
	Quaternary structure involves the interaction of subunits in a protein with more than one polypeptide chain.

maroonwallaby335

The sequence of amino acids is considered to be the ________ structure of a protein.

Select one:

a. secondary

b. tertiary

c. quaternary

d. primary

The pattern the backbone folds, for example alpha-helix or beta pleated sheet, is the ________ structure of a protein.

Select one:

a. quaternary

b. secondary

c. tertiary

d. primary

Which type of forces stabilizes the primary structure of a protein?

Select one:

a. Salt bridges

b. Hydrogen bonding between the carbonyl group and amino group

c. Dipole-dipole

d. Peptide bonds

The interaction of the side chains on the amino acids, for example hydrophobic attractions, is the ________ structure of a protein.

Select one:

a. quaternary

b. secondary

c. tertiary

d. primary

violetyellowjacket662

1. In biology, the term "ionic bond" is used differently than inchemistry. A biological "ionic bond" is used to describe theinteraction of an R group containing a carboxyl group(âCOO^â) with an R group containing an amino group(âNH₃⁺). From this description, what do youunderstand a biological "ionic bond" to be?

a. van der waals interaction

b. hydrogen bond

c. Electrostatic interaction

d. covalent bond

2. The three dimensional arrangement of alpha helices,beta-sheets and other parts of the polypeptide chain is called

a. primary structure

b. secondary strucutre

c. tertiary structure

d. quaternary structure

3. Multiple polypeptide chains are held together by

a. peptide bond

b. intermolecular forces

4. What holds multiple polypeptides together? (Choose bestanswer)

a. R groups

b. amino groups

c. carboxylate group

5. Which of the following single-celled organisms is an exampleof a prokaryote?

a. algae

b. yeast

c. amoeba

d. bacteria

6. Which of the following is an insect most closely relatedto?

a. tree

b. mushroom

c. fish

d. bacteria

7. In evolutionary history, which was the most ancientdivergence?

a. Prokaryotes and eukaryotes

b. Birds and reptiles

c. Rats and mice

d. Plants and animals

8. In evolutionary history, which was the most recentdivergence?

a. Prokaryotes and eukaryotes

b. Birds and reptiles

c. Rats and mice

d. Plants and animals

9. What is the chemical equation for ATP synthesis?

a. ADP + P_i â¶ ATP + H₂O

b. ATP + H₂O â¶ ADP + P_i

_c. ADP + H₂O â¶ ATP + P_i

_d. ATP + P_i â¶ ADP +H₂O

9. What is glycolysis?]

a. It is the oxidation of three-carbon molecules into carbondioxide.

b. It is the splitting of six-carbon sugars into three carbonmolecules with the synthesis of ATP.

c. It is the transport of electrons to power the synthesis ofATP.

d. It is the synthesis of sugars from carbon dioxide.

10. What chemistry concept describes whether a reaction orprocess can occur spontaneously?

a. therodynamics

b. kinetics

mauvetortoise304

BSCI-1510 Lecture Notes - Lecture 5: Beta Barrel, Ribbon Diagram, Alpha Helix

Document Summary

Get access

Related Documents

BSCI-1510 Lecture 3: Kendal Broadie- Protein Structure, Folding, and Function- August 29th, 2018

BSCI-1510 Lecture Notes - Lecture 22: Alcohol Dehydrogenase, Glycosidic Bond, Nucleosome

BIOCHEM 2EE3 Lecture Notes - Lecture 2: Aldehyde, Lysine, Ultimate Tensile Strength

Related Questions